Our original research plan was to study the globin gene-protein complex which is insoluble in 2M NaCl based on the report by Bekhor and Mirrel (Biochemistry 18 (1978) 609) on the enrichment of the globin genes in the chromatin fraction which remains insoluble in 2M NaCl after repeated shearing and centrifugations. We found that this 2M NaCl-insoluble fraction is in fact the nuclear matrix, and instead of the globin gene enrichment all of the nuclear globin RNA are tightly bound. Both precursor and processed glogin RNA are enriched in the matrix and the matrix-binding sites in the RNA are specific. These binding sites are resistant to micrococcal nuclease and the nuclease produces globin RNA fragments in multiples of 16 bases. The same results are obtained with whole nuclei. We are in the process of determining the nucleotide sequences of the globin RNA interacting with the nuclear matrix. Our results suggest that the globin RNA is processed at the nuclear matrix. Also there are several precursor globin RNA's ranging from 2000 to 6000 bases long, and if the RNA's extend toward 3' of the globin genes there is possibility that the precursor RNA's run into the adjacent globin genes. This possibility is being investigated.